3s4x

Crystal structure of the Asn152Gly mutant of P99 beta-lactamaseCrystal structure of the Asn152Gly mutant of P99 beta-lactamase

Structural highlights 3s4x is a 1 chain structure with sequence from Enterobacter cloacae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Gene: ampC (Enterobacter cloacae) Activity: Beta-lactamase, with EC number 3.5.2.6 Resources: FirstGlance, OCA, RCSB, PDBsum Function [AMPC_ENTCL] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. Publication Abstract from PubMed P99 cephalosporinase is a class C beta-lactamase that is responsible in part for the widespread bacterial resistance to beta-lactam antibiotics. Mutations of the conserved active-site residue Asn152 of the enzyme have been shown to alter beta-lactam substrate specificity in vivo. Mutation of Asn152 to a glycine is notable in that it exhibits in vivo substrate-selectivity switching. In order to better understand the structural basis for this observed switch, the X-ray crystal structure of the apo Asn152Gly mutant of P99 was determined to 1.95 A resolution. Unexpectedly, the artificial C-terminal His(6) tag of a symmetrically-related molecule was observed bound in the active site. The His(6) tag makes several interactions with key active-site residues, as well as with several sulfate ions. Additionally, the overall C-terminus occupies the space left vacant upon the mutation of Asn152 to glycine. Structural analysis of the Asn152Gly mutant of P99 cephalosporinase.,Ruble JF, Lefurgy ST, Cornish VW, Powers RA Acta Crystallogr D Biol Crystallogr. 2012 Sep;68(Pt 9):1189-93. doi:, 10.1107/S0907444912024080. Epub 2012 Aug 18. PMID:22948919 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Beta-lactamase

spinqualitylabelsall models 3s4x, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image